4B4W
Crystal structure of Acinetobacter baumannii N5, N10- methylenetetrahydrofolate dehydrogenase-cyclohydrolase (FolD) complexed with NADP cofactor and an inhibitor
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000105 | biological_process | L-histidine biosynthetic process |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0004477 | molecular_function | methenyltetrahydrofolate cyclohydrolase activity |
| A | 0004488 | molecular_function | methylenetetrahydrofolate dehydrogenase (NADP+) activity |
| A | 0005829 | cellular_component | cytosol |
| A | 0006164 | biological_process | purine nucleotide biosynthetic process |
| A | 0006730 | biological_process | one-carbon metabolic process |
| A | 0008652 | biological_process | amino acid biosynthetic process |
| A | 0009086 | biological_process | methionine biosynthetic process |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0035999 | biological_process | tetrahydrofolate interconversion |
| B | 0000105 | biological_process | L-histidine biosynthetic process |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0004477 | molecular_function | methenyltetrahydrofolate cyclohydrolase activity |
| B | 0004488 | molecular_function | methylenetetrahydrofolate dehydrogenase (NADP+) activity |
| B | 0005829 | cellular_component | cytosol |
| B | 0006164 | biological_process | purine nucleotide biosynthetic process |
| B | 0006730 | biological_process | one-carbon metabolic process |
| B | 0008652 | biological_process | amino acid biosynthetic process |
| B | 0009086 | biological_process | methionine biosynthetic process |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0035999 | biological_process | tetrahydrofolate interconversion |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE NAP A 1001 |
| Chain | Residue |
| A | ARG166 |
| A | HOH2142 |
| A | HOH2219 |
| A | HOH2231 |
| A | HOH2244 |
| A | HOH2289 |
| A | HOH2290 |
| A | HOH2292 |
| A | HOH2293 |
| A | SER167 |
| A | HIS189 |
| A | SER190 |
| A | LEU195 |
| A | ALA208 |
| A | VAL209 |
| A | LYS211 |
| A | LEU214 |
| site_id | AC2 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE 9L9 A 2001 |
| Chain | Residue |
| A | TYR49 |
| A | MET52 |
| A | LYS53 |
| A | LEU95 |
| A | LEU96 |
| A | GLN97 |
| A | HIS98 |
| A | ASP120 |
| A | PHE231 |
| A | PRO258 |
| A | GLY259 |
| A | GLY262 |
| A | PRO263 |
| A | THR265 |
| A | HOH2096 |
| A | HOH2195 |
| A | HOH2275 |
| A | HOH2277 |
| A | HOH2295 |
| site_id | AC3 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE NAP B 1001 |
| Chain | Residue |
| B | ARG166 |
| B | HIS189 |
| B | SER190 |
| B | ALA208 |
| B | VAL209 |
| B | LYS211 |
| B | LEU214 |
| B | HOH2224 |
| B | HOH2237 |
| B | HOH2288 |
| B | HOH2289 |
| B | HOH2290 |
| B | HOH2291 |
| B | HOH2293 |
| site_id | AC4 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE 9L9 B 2001 |
| Chain | Residue |
| A | LYS12 |
| B | TYR49 |
| B | MET52 |
| B | LYS53 |
| B | LEU95 |
| B | LEU96 |
| B | GLN97 |
| B | HIS98 |
| B | ASP120 |
| B | PHE231 |
| B | PRO258 |
| B | GLY259 |
| B | GLY262 |
| B | PRO263 |
| B | THR265 |
| B | HOH2093 |
| B | HOH2189 |
| B | HOH2270 |
| B | HOH2272 |
| B | HOH2295 |
| B | HOH2297 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL A 1283 |
| Chain | Residue |
| A | ALA136 |
| A | ARG271 |
| A | GLN272 |
| A | GLU275 |
| A | HOH2191 |
| site_id | AC6 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE GOL B 1283 |
| Chain | Residue |
| B | GLU76 |
| B | HOH2118 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL A 1284 |
| Chain | Residue |
| A | ARG59 |
| A | HOH2097 |
| B | ARG59 |
Functional Information from PROSITE/UniProt
| site_id | PS00136 |
| Number of Residues | 12 |
| Details | SUBTILASE_ASP Serine proteases, subtilase family, aspartic acid active site. AVVVDAGFhprD |
| Chain | Residue | Details |
| A | ALA224-ASP235 |
| site_id | PS00767 |
| Number of Residues | 9 |
| Details | THF_DHG_CYH_2 Tetrahydrofolate dehydrogenase/cyclohydrolase signature 2. PGGVGPMTI |
| Chain | Residue | Details |
| A | PRO258-ILE266 |
